1Y3J
Solution structure of the copper(I) form of the fifth domain of Menkes protein
Summary for 1Y3J
| Entry DOI | 10.2210/pdb1y3j/pdb |
| Related | 1Y3K |
| Descriptor | Copper-transporting ATPase 1, COPPER (II) ION (2 entities in total) |
| Functional Keywords | ferrodoxin-like fold, beta-alpha-beta-beta-alpha-beta structure, structural proteomics in europe, spine, structural genomics, hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Isoform 3: Cytoplasm, cytosol (Probable). Isoform 5: Endoplasmic reticulum: Q04656 |
| Total number of polymer chains | 1 |
| Total formula weight | 8549.39 |
| Authors | Banci, L.,Chasapis, C.T.,Ciofi-Baffoni, S.,Hadjiliadis, N.,Rosato, A.,Structural Proteomics in Europe (SPINE) (deposition date: 2004-11-25, release date: 2005-03-08, Last modification date: 2024-05-29) |
| Primary citation | Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Chasapis, C.T.,Hadjiliadis, N.,Rosato, A. An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein Febs J., 272:865-871, 2005 Cited by PubMed Abstract: The interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein (ATP7A), was investigated in solution using heteronuclear NMR. The study was carried out through titrations involving HAH1 and either the second or the fifth soluble domains of ATP7A (MNK2 and MNK5, respectively), in the presence of copper(I). The copper-transfer properties of MNK2 and MNK5 are similar, and differ significantly from those previously observed for the yeast homologous system. In particular, no stable adduct is formed between either of the MNK domains and HAH1. The copper(I) transfer reaction is slow on the time scale of the NMR chemical shift, and the equilibrium is significantly shifted towards the formation of copper(I)-MNK2/MNK5. The solution structures of both apo- and copper(I)-MNK5, which were not available, are also reported. The results are discussed in comparison with the data available in the literature for the interaction between HAH1 and its partners from other spectroscopic techniques. PubMed: 15670166DOI: 10.1111/j.1742-4658.2004.04526.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
